We are investigating the structure and dynamics of sequence specific heteropolymers. Through a collaborative effort between the labs of Ken Dill and Fred Cohen at UCSF, and the Drug Discovery group at Chiron Corporation, we have been able to synthesize N-substituted glycine polymers of 5 to 30 residues containing sidechains with diverse chemical functionalities. By NMR and circular dichroic spectroscopy, we have established that these molecules self-assemble into helical secondary structures. We believe that by variation of the precise sequence of these peptoid oligomers, we can generate macromolecules that fold into well-defined and stable tertiary conformations. Access to the computer graphics laboratory will allow the user to visualize and better understand the structures now being elucidated by NMR. In addition, I intend to pursue computer-assisted molecular design to understand the relationship between primary sequence and tertiary conformation in this system. This will involve both energy calculations on static structures and molecular dynamics simulations. It is anticipated that this will allow for a better understanding of the driving forces for protein folding, and should provide the groundwork for the synthesis of a new class of biologically inspired materials that are responsive to signalling.